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http://purl.uniprot.org/citations/1833064http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1833064http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1833064http://www.w3.org/2000/01/rdf-schema#comment"A cDNA for a human interleukin-3 (hIL-3) binding protein has been isolated by a novel expression cloning strategy: a cDNA library was coexpressed with the cDNA for the beta subunit of human granulocyte/macrophage colony-stimulating factor (GM-CSF) receptor (hGMR beta) in COS7 cells and screened by binding of 125I-labeled IL-3. The cloned cDNA (DUK-1) encodes a mature protein of 70 kd, which belongs to the cytokine receptor family and which alone binds hIL-3 with extremely low affinity (Kd = 120 +/-60 nM). A high affinity IL-3-binding site (Kd = 140 +/-30 pM) was reconstituted by coexpressing the DUK-1 protein and hGMR beta, indicating that hIL-3R and hGMR share the beta subunit. Therefore, we designated DUK-1 as the alpha subunit of the hIL-3R. As in human hematopoietic cells, hIL-3 and hGM-CSF complete for binding in fibroblasts expressing the cDNAs for hIL-3R alpha, GMR alpha, and the common beta subunit, indicating that different alpha subunits compete for a common beta subunit."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(91)90039-2"xsd:string
http://purl.uniprot.org/citations/1833064http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(91)90039-2"xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/author"Arai K."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/author"Arai K."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/author"Sato N."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/author"Sato N."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/author"Kitamura T."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/author"Kitamura T."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/author"Miyajima A."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/author"Miyajima A."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/pages"1165-1174"xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/pages"1165-1174"xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/title"Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/title"Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors."xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/1833064http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/1833064http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1833064
http://purl.uniprot.org/citations/1833064http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1833064